Calcium in PDB 6ry0: Crystal Structure of DFG5 From Chaetomium Thermophilum

All present enzymatic activity of Crystal Structure of DFG5 From Chaetomium Thermophilum:
3.2.1.101;

The structure of Crystal Structure of DFG5 From Chaetomium Thermophilum, PDB code: 6ry0 was solved by L.-O.Essen, M.S.Vogt, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	30.28 / 1.05
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	83.319, 54.989, 80.416, 90.00, 90.27, 90.00
R / Rfree (%)	10.6 / 12.3

The binding sites of Calcium atom in the Crystal Structure of DFG5 From Chaetomium Thermophilum (pdb code 6ry0). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total only one binding site of Calcium was determined in the Crystal Structure of DFG5 From Chaetomium Thermophilum, PDB code: 6ry0:

Calcium binding site 1 out of 1 in the Crystal Structure of DFG5 From Chaetomium Thermophilum


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Crystal Structure of DFG5 From Chaetomium Thermophilum within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca502 b:10.7 occ:0.54 O A:HOH795 2.1 28.2 1.0 OD1 A:ASP79 2.3 13.5 1.0 O A:HOH949 2.3 23.5 1.0 O A:HOH979 2.4 27.4 1.0 O A:HIS391 2.5 14.3 1.0 O A:HOH711 2.5 34.5 1.0 CG A:ASP79 3.4 10.9 1.0 C A:HIS391 3.6 12.5 1.0 HA A:THR392 3.6 12.4 1.0 HB3 A:HIS391 3.7 19.0 1.0 HA A:ASP79 3.9 11.6 1.0 HB3 A:ASP79 4.2 11.5 1.0 OD2 A:ASP79 4.3 11.7 1.0 O A:HOH1034 4.3 40.5 1.0 CB A:ASP79 4.3 9.6 1.0 HG22 A:THR392 4.4 13.5 1.0 CB A:HIS391 4.4 15.8 1.0 HB2 A:HIS391 4.4 19.0 1.0 O A:HOH707 4.4 20.3 1.0 CA A:THR392 4.5 10.3 1.0 N A:THR392 4.5 10.6 1.0 CA A:HIS391 4.5 13.0 1.0 O A:HOH671 4.6 23.6 1.0 CA A:ASP79 4.6 9.7 1.0 HA A:HIS391 4.6 15.6 1.0 O A:HOH951 4.8 26.5 1.0 HB3 A:PRO73 4.9 18.2 1.0

M.S.Vogt, G.F.Schmitz, D.Varon Silva, H.U.Mosch, L.O.Essen. Structural Base For the Transfer of Gpi-Anchored Glycoproteins Into Fungal Cell Walls. Proc.Natl.Acad.Sci.Usa V. 117 22061 2020.
ISSN: ESSN 1091-6490
PubMed: 32839341
DOI: 10.1073/PNAS.2010661117